The protein synthesized i
The protein synthesized in the most copies in E. coli is an alpha helix rich lipoprotein discovered by Braun; one-third of those copies bind covalently through the C-terminal lysine to this substance. The topical antibiotic bacitracin inhibits the function of bactoprenol in the synthesis of this substance, and NOD1 recognizes meso-DAP, which is found here. Teichoic acids and this substance bind to surface layer homology domains. A pseudo-form of this substance features beta-(1,3) linkage and leads to the lysozyme-insensitivity of Archea. Penicillin-binding proteins are essential in the synthesis of this substance, which is one of few natural occurrences of D-amino acids. One component of this substance consists of alternating NAG and NAM linkages, the latter of which hosts a three to five amino acid sequence. For 10 points, name this polymer of sugars and amino acids also called murein, which is found in particularly large amounts in Gram-positive bacteria and which forms the cell wall.
The protein synthesized in the most copies in E. coli is an alpha helix rich lipoprotein discovered by Braun; one-third of those copies bind covalently through the C-terminal lysine to this substance.
{peptidoglycan} [accept {murein} before mention]